Receptor
PDB id Resolution Class Description Source Keywords
2PV1 1.3 Å EC: 5.2.1.8 CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISO DOMAIN COMPLEXED WITH PEPTIDE WEYIPNV ESCHERICHIA COLI SURVIVAL PROTEIN A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE DOMACOMPLEX ISOMERASE
Ref.: THE PERIPLASMIC BACTERIAL MOLECULAR CHAPERONE SURA ITS STRUCTURE TO BIND PEPTIDES IN DIFFERENT CONFORM ASSERT A SEQUENCE PREFERENCE FOR AROMATIC RESIDUES. J.MOL.BIOL. V. 373 367 2007
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
TRP GLU TYR ILE PRO ASN VAL B:1;
 Valid;
 none;
 Kd = 0.073 uM
919.026 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2PV1 1.3 Å EC: 5.2.1.8 CRYSTALLOGRAPHIC STRUCTURE OF SURA FIRST PEPTIDYL-PROLYL ISO DOMAIN COMPLEXED WITH PEPTIDE WEYIPNV ESCHERICHIA COLI SURVIVAL PROTEIN A PEPTIDYL-PROLYL CIS-TRANS ISOMERASE DOMACOMPLEX ISOMERASE
Ref.: THE PERIPLASMIC BACTERIAL MOLECULAR CHAPERONE SURA ITS STRUCTURE TO BIND PEPTIDES IN DIFFERENT CONFORM ASSERT A SEQUENCE PREFERENCE FOR AROMATIC RESIDUES. J.MOL.BIOL. V. 373 367 2007
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 30 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
70% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 20 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
50% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 13 families.
1 2PV1 Kd = 0.073 uM TRP GLU TYR ILE PRO ASN VAL n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: TRP GLU TYR ILE PRO ASN VAL; Similar ligands found: 161
No: Ligand ECFP6 Tc MDL keys Tc
1 TRP GLU TYR ILE PRO ASN VAL 1 1
2 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.566879 0.910448
3 MET TYR TRP TYR PRO TYR 0.558442 0.84507
4 MET VAL TRP GLY PRO ASP PRO LEU TYR VAL 0.544944 0.876712
5 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.530726 0.898551
6 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.521212 0.911765
7 ALA PRO ALA TRP LEU PHE GLU ALA 0.515152 0.867647
8 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.514793 0.926471
9 ASN ASP TRP LEU LEU PRO SER TYR 0.51462 0.929577
10 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.514286 0.914286
11 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.511111 0.813333
12 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.509091 0.876712
13 LEU LEU TRP ASN GLY PRO MET GLN VAL 0.5 0.847222
14 THR PRO TYR ASP ILE ASN GLN MET LEU 0.5 0.849315
15 SER PRO LEU ASP SER LEU TRP TRP ILE 0.5 0.887324
16 ALA VAL PRO TRP 0.492958 0.835821
17 TYR TYR SER ILE ILE PRO HIS SER ILE 0.490798 0.888889
18 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.489474 0.824324
19 TRP GLU GLU LEU 0.488889 0.701493
20 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.485549 0.898551
21 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.484848 0.73494
22 LEU LEU TRP ASN GLY PRO ILE ALA VAL 0.482353 0.911765
23 MET LEU TRP GLY TYR LEU GLN TYR VAL 0.481928 0.763889
24 PRO GLN PTR GLU GLU ILE PRO ILE 0.481707 0.763158
25 ARG TYR PRO LEU THR PHE GLY TRP 0.481081 0.866667
26 ARG GLN TRP GLY PRO ASP PRO ALA ALA VAL 0.481081 0.773333
27 ALA TRP VAL ILE PRO ALA 0.47973 0.823529
28 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.479167 0.866667
29 PRO GLN PTR GLU PTR ILE PRO ALA 0.478788 0.789474
30 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.477012 0.942029
31 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.476744 0.888889
32 ASP TRP GLU ILE VAL 0.47619 0.716418
33 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.47561 0.867647
34 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.47093 0.956522
35 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.469613 0.830986
36 TRP PRO TRP 0.467626 0.791045
37 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.466667 0.867647
38 GLN ASN TYR PRO ILE VAL GLN 0.465409 0.925373
39 ACE TYR PRO ILE GLN GLU THR 0.465409 0.84058
40 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.464088 0.807692
41 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.463687 0.8
42 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.462963 0.792208
43 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.462857 0.867647
44 GLN ILE MET TYR ASN TYR PRO ALA MET 0.461988 0.901408
45 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.461538 0.897059
46 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.461538 0.813333
47 LEU LEU TRP ASN GLY PRO MET ALA VAL 0.460674 0.847222
48 GLY GLU GLU TRP GLY PRO TRP VAL NH2 0.459627 0.852941
49 ILE MET ASP GLN VAL PRO PHE SER VAL 0.459302 0.76
50 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.457317 0.869565
51 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.457317 0.859155
52 PHE ASN PHE PRO GLN ILE THR 0.45625 0.869565
53 GLU PRO GLN ALA PRO TRP MET GLU GLN 0.45614 0.780822
54 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.454545 0.911765
55 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.454545 0.738095
56 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.454545 0.871429
57 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.453947 0.835821
58 TYR TYR SER ILE ALA PRO HIS SER ILE 0.452941 0.863014
59 ILE THR ASP GLN VAL PRO PHE SER VAL 0.452941 0.816901
60 ALA THR PRO PHE GLN GLU 0.451613 0.794118
61 ACE GLN PM3 GLU GLU ILE PRO 0.451613 0.72973
62 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.449704 0.888889
63 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.449438 0.815789
64 ASN GLN DPR TRP GLN 0.449367 0.820895
65 TRP ASN TRP PHE ASP ILE THR ASN LYS 0.449102 0.753623
66 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.448864 0.914286
67 THR ASN GLU TYR TYR VAL 0.448529 0.701493
68 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.446927 0.84058
69 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.445652 0.797297
70 SER VAL TYR ASP PHE PHE VAL TRP LEU 0.445122 0.746479
71 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.445087 0.859155
72 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.444444 0.844156
73 ALA GLN TRP GLY PRO ASP PRO ALA ALA ALA 0.44382 0.826087
74 GLN MET PRO THR GLU ASP GLU TYR 0.443787 0.821918
75 PHE SER ASP PRO TRP GLY GLY 0.443787 0.816901
76 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.44375 0.830986
77 ARG PHE PRO LEU THR PHE GLY TRP 0.443243 0.84
78 ASP ILE ASN TYR TYR THR SER GLU PRO 0.443114 0.887324
79 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.442424 0.859155
80 LEU PHE GLY TYR PRO VAL TYR VAL 0.442424 0.882353
81 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.442105 0.78481
82 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.441176 0.773333
83 GLU PRO VAL GLU THR THR ASP TYR 0.440994 0.855072
84 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.440678 0.777778
85 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.440678 0.867647
86 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.440476 0.887324
87 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.44 0.871429
88 ACE ASN TRP GLU THR PHE 0.43949 0.714286
89 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.439024 0.690141
90 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.437126 0.830986
91 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.436464 0.842105
92 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.436364 0.898551
93 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.435583 0.84507
94 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.435294 0.882353
95 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.435294 0.882353
96 ALA SER LEU ASN LEU PRO ALA VAL SER TRP 0.435028 0.873239
97 HIS SER ILE THR TYR LEU LEU PRO VAL 0.435028 0.888889
98 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.433526 0.808824
99 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.433526 0.884058
100 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.431953 0.927536
101 ALA PRO SER PTR VAL ASN VAL GLN ASN 0.431953 0.759494
102 LEU LEU TRP ALA GLY PRO MET ALA VAL 0.431818 0.794521
103 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.431579 0.779221
104 PHE SER HIS PRO GLN ASN THR 0.429412 0.819444
105 GLY LEU MET TRP LEU SER TYR PHE VAL 0.429412 0.756757
106 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.429348 0.783784
107 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.428571 0.898551
108 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.427861 0.831169
109 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.427778 0.753247
110 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.427778 0.802632
111 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.427673 0.84058
112 ASP ASP TRP ASN TRP GLU VAL GLU ASP 0.427632 0.735294
113 TRP ASP ILE PRO PHE 0.427586 0.80597
114 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.427083 0.797468
115 SER SER VAL ILE GLY VAL TRP TYR LEU 0.426901 0.774648
116 ALA TRP ARG HIS PRO GLN PHE GLY GLY 0.426316 0.77027
117 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.425641 0.777778
118 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.425414 0.871429
119 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.425287 0.914286
120 LEU PRO SER PHE GLU THR ALA LEU 0.42515 0.802817
121 SER TRP PHE PRO 0.424837 0.814286
122 TYR GLU TRP 0.423611 0.701493
123 ASP ASN ARG LEU GLY LEU VAL TYR TRP PHE 0.422819 0.716418
124 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.422111 0.790123
125 SER PRO ILE VAL PRO SER PHE ASP MET 0.421965 0.786667
126 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.420765 0.898551
127 GLY SER ASP PRO TRP LYS 0.420732 0.802817
128 PRO ALA TRP ASP GLU THR ASN LEU 0.41954 0.814286
129 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.419355 0.717949
130 THR ASN GLU TYR LYS VAL 0.418919 0.720588
131 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.418605 0.884058
132 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.418605 0.871429
133 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.415842 0.790123
134 MET HIS PRO ALA GLN THR SER GLN TRP 0.415789 0.815789
135 GLY SER HIS LEU GLU VAL GLN GLY TYR TRP 0.414894 0.830986
136 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.414141 0.818182
137 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.413793 0.767123
138 ALA PHE ARG ILE PRO LEU THR ARG 0.413793 0.763158
139 ALA SER ASN GLU ASN TRP GLU THR MET 0.412121 0.693333
140 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.412088 0.824324
141 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.411765 0.802632
142 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.410714 0.871429
143 PRO ALA TRP LEU PHE GLU ALA 0.409357 0.779412
144 LYS GLN TRP LEU VAL TRP LEU PHE LEU 0.409357 0.764706
145 MDL 0.409091 0.68
146 GLU GLN TYR LYS PHE TYR SER VAL 0.408805 0.728571
147 SER SER VAL VAL GLY VAL TRP TYR LEU 0.408284 0.760563
148 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.407609 0.914286
149 ABA SER LEU TRP ASN GLY PRO HIS LEU 0.407609 0.875
150 ALA ALA TRP LEU PHE GLU ALA 0.407407 0.701493
151 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.406593 0.818182
152 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.40625 0.880597
153 ALA TRP LEU PHE GLU ALA 0.405063 0.701493
154 THR SER ASN LEU GLN GLU GLN ILE GLY TRP 0.404494 0.788732
155 GLU GLU ASN ASP PRO ASP TYR 0.403974 0.838235
156 PHE ASN ARG PRO VAL 0.403727 0.743243
157 SER ARG TYR TRP ALA ILE ARG THR ARG 0.403315 0.727273
158 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.401099 0.789474
159 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.4 0.865672
160 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.4 0.8
161 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.4 0.842105
Similar Ligands (3D)
Ligand no: 1; Ligand: TRP GLU TYR ILE PRO ASN VAL; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader) APoc FAQ
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